Structure of PDB 2c2b Chain C

Receptor sequence
>2c2bC (length=443) Species: 3702 (Arabidopsis thaliana) [Search protein sequence]
NPFSAKYVPFNAAPGSTESYSLDEIVYRSRSGGLLDVEHDMEALKRFDGA
YWRDLFDSRVGKSTWPYGSGVWSKKEWVLPEIDDDDIVSAFEGNSNLFWA
ERFGKQFLGMNDLWVKHCGISHTGSFKDLGMTVLVSQVNRLRKMKRPVVG
VGCASTGDTSAALSAYCASAGIPSIVFLPANKISMAQLVQPIANGAFVLS
IDTDFDGCMKLIREITAELPIYLANSLNSLRLEGQKTAAIEILQQFDWQV
PDWVIVPGGNLGNIYAFYKGFKMCQELGLVDRIPRMVCAQAANANPLYLH
YKSGWKDFKPMTASTTFASAIQIGDPVSIDRAVYALKKCNGIVEEATEEE
LMDAMAQADSTGMFICPHTGVALTALFKLRNQGVIAPTDRTVVVSTAHGL
KFTQSKIDYHSNAIPDMACRFSNPPVDVKADFGAVMDVLKSYL
3D structure
PDB2c2b Allosteric Threonine Synthase: Reorganization of the Pyridoxal Phosphate Site Upon Asymmetric Activation Through S-Adenosylmethionine Binding to a Novel Site.
ChainC
Resolution2.6 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 4.2.3.1: threonine synthase.
Interaction with ligand
Site
#
Ligand Ligand
chain
Binding residues on receptor
(original residue number in PDB)
Binding residues on receptor
(residue number reindexed from 1)
Binding affinity
BS01 SAM C S99 T100 W101 P102 G104 S105 F127 S63 T64 W65 P66 G68 S69 F91
BS02 PLP C F162 K163 D194 G294 G295 N296 L297 G298 N299 A356 H404 T432 F126 K127 D158 G258 G259 N260 L261 G262 N263 A320 H368 T396
BS03 SAM C N132 L133 W150 Q281 F282 N96 L97 W114 Q245 F246
BS04 SAM C W135 W150 W99 W114
Gene Ontology
Molecular Function
GO:0004795 threonine synthase activity
GO:0016829 lyase activity
GO:0030170 pyridoxal phosphate binding
Biological Process
GO:0006520 amino acid metabolic process
GO:0009088 threonine biosynthetic process
Cellular Component
GO:0005886 plasma membrane
GO:0009507 chloroplast
GO:0009570 chloroplast stroma

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:2c2b, PDBe:2c2b, PDBj:2c2b
PDBsum2c2b
PubMed16319072
UniProtQ9S7B5|THRC1_ARATH Threonine synthase 1, chloroplastic (Gene Name=TS1)

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